ID   ABNA_ASPAC              Reviewed;         321 AA.
AC   Q9HFS9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Arabinan endo-1,5-alpha-L-arabinosidase A;
DE            EC=3.2.1.99;
DE   AltName: Full=Endo-1,5-alpha-L-arabinanase A;
DE            Short=ABN A;
DE   Flags: Precursor;
GN   Name=abnA; Synonyms=ara1;
OS   Aspergillus aculeatus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-38, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=CBS 101.43;
RX   PubMed=11523809; DOI=10.1007/s004380100489;
RA   Skjoet M., Kauppinen S., Kofod L.V., Fuglsang C.C., Pauly M., Dalboege H.,
RA   Andersen L.N.;
RT   "Functional cloning of an endo-arabinanase from Aspergillus aculeatus and
RT   its heterologous expression in A. oryzae and tobacco.";
RL   Mol. Genet. Genomics 265:913-921(2001).
CC   -!- FUNCTION: Endo-1,5-alpha-L-arabinanase involved in degradation of
CC       pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:11523809}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC         (1->5)-arabinans.; EC=3.2.1.99;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=66 mM for AZCL-debranched arabinan {ECO:0000269|PubMed:11523809};
CC       pH dependence:
CC         Optimum pH is 5.5. Stable between pH 5.5 and 6.5.
CC         {ECO:0000269|PubMed:11523809};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:11523809};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; AF300878; AAG27441.1; -; mRNA.
DR   AlphaFoldDB; Q9HFS9; -.
DR   SMR; Q9HFS9; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   CLAE; ABN43A_ASPAC; -.
DR   VEuPathDB; FungiDB:ASPACDRAFT_53126; -.
DR   UniPathway; UPA00667; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..321
FT                   /note="Arabinan endo-1,5-alpha-L-arabinosidase A"
FT                   /id="PRO_5000058634"
FT   ACT_SITE        34
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   SITE            149
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  34097 MW;  FAE9D565631613F1 CRC64;
     MYSLLTALSV PLLAGLAHGY ANPGSCSGSC NVHDPALIVR ESDGKYFRFS TGNEISYASA
     SSINGPWTAI GSVVPAGSKI DLSGNTDLWA PDLSYVDGTY YCLYSVSTFG SQDSAIGVAS
     STTMELNTWT DHGSVGVASS SSKNYNAIDG NLLVDGSSYY LQFGSFWGDI YQVKMASPLK
     TAGSASYNIA YNATGTHSEE GSYLFKYGSY YYLFFSSGTC CGYDTSRPAQ GEEYKIMVCR
     STSATGGFVD KNGNACTESG GTIVLASHGT VYGPGGQGVY DDPTYGPVLY YHYVDTTIGY
     ADDQKLFGWN TIDFSSGWPV V